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Protein adsorption on derivatives of hyaluronic acid and subsequent cellular response
Author(s) -
Lord Megan S.,
Pasqui Daniela,
Barbucci Rolando,
Milthorpe Bruce K.
Publication year - 2008
Publication title -
journal of biomedical materials research part a
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.849
H-Index - 150
eISSN - 1552-4965
pISSN - 1549-3296
DOI - 10.1002/jbm.a.32219
Subject(s) - fibronectin , quartz crystal microbalance , hyaluronic acid , adhesion , cell adhesion , adsorption , protein adsorption , biophysics , materials science , cell , albumin , polymer , biochemistry , chemistry , organic chemistry , biology , anatomy , composite material
The modulation of biological interactions with artificial surfaces is a vital aspect of biomaterials research. Serum protein adsorption onto photoreactive hyaluronic acid (Hyal‐N 3 ) and its sulfated derivative (HyalS‐N 3 ) was analyzed to determine extent of protein interaction and protein conformation as well as subsequent cell adhesion. There were no significant ( p < 0.01) differences in the amount of protein adsorbed to the two polymers; however, proteins were found to be more loosely bound on HyalS‐N 3 compared with Hyal‐N 3 . Fibronectin was adsorbed onto HyalS‐N 3 in such an orientation as to allow the availability of the cell binding region, while there was more restricted access to this region on fibronectin adsorbed onto Hyal‐N 3 . This was confirmed by reduced cell adhesion on fibronectin precoated Hyal‐N 3 compared with fibronectin precoated HyalS‐N 3 . Minimal cell adhesion was observed on albumin and serum precoated Hyal‐N 3 . The quartz crystal microbalance confirmed that specific cell‐surface interactions were experienced by cells interacting with the fibronectin precoated polymers and serum precoated HyalS‐N 3 . © 2008 Wiley Periodicals, Inc. J Biomed Mater Res, 2009